Structure of PDB 1iew Chain A

Receptor sequence
>1iewA (length=602) Species: 4513 (Hordeum vulgare) [Search protein sequence]
DYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFI
GSLLSGGGSVPRKGATAKEWQDMVDGFQKACMSTRLGIPMIYGIDAVHGQ
NNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAV
CRDPRWGRCYESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNK
VAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKNAMDKGVSTVM
ISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDY
SYSVKASILAGLDMIMVPNKYQQFISILTGHVNGGVIPMSRIDDAVTRIL
RVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGKTSTD
APLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTTILEA
VKAAVDPSTVVVFAENPDAEFVKSGGFSYAIVAVGEHPYTETKGDNLNLT
IPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEG
QGVTDALFGDFGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTN
AT
3D structure
PDB1iew Catalytic mechanisms and reaction intermediates along the hydrolytic pathway of a plant beta-D-glucan glucohydrolase.
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D285 E491
Catalytic site (residue number reindexed from 1) D285 E491
Enzyme Commision number 3.2.1.21: beta-glucosidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 G2F A D95 R158 K206 H207 Y253 D285 W286 M316 D95 R158 K206 H207 Y253 D285 W286 M316 PDBbind-CN: -logKd/Ki=4.59,Ki=25.50uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1iew, PDBe:1iew, PDBj:1iew
PDBsum1iew
PubMed11709165
UniProtQ9XEI3

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